ID B9U765_9NEOP Unreviewed; 427 AA.
AC B9U765;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Aromatic-L-amino-acid decarboxylase {ECO:0000256|ARBA:ARBA00040968};
DE EC=4.1.1.28 {ECO:0000256|ARBA:ARBA00038886};
DE AltName: Full=DOPA decarboxylase {ECO:0000256|ARBA:ARBA00041275};
DE Flags: Fragment;
GN Name=DDC {ECO:0000313|EMBL:ACD01600.1};
OS Euryglottis dognini.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Euryglottis.
OX NCBI_TaxID=522826 {ECO:0000313|EMBL:ACD01600.1};
RN [1] {ECO:0000313|EMBL:ACD01600.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AToL-Lep-ID WJK-03-2891 {ECO:0000313|EMBL:ACD01600.1};
RX PubMed=19492095; DOI=10.1371/journal.pone.0005719;
RA Kawahara A.Y., Mignault A.A., Regier J.C., Kitching I.J., Mitter C.;
RT "Phylogeny and biogeography of hawkmoths (Lepidoptera: Sphingidae):
RT evidence from five nuclear genes.";
RL PLoS ONE 4:e5719-e5719(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR EMBL; EU479170; ACD01600.1; -; mRNA.
DR AlphaFoldDB; B9U765; -.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0042423; P:catecholamine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010977; Aromatic_deC.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 2: Evidence at transcript level;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382}.
FT MOD_RES 274
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACD01600.1"
FT NON_TER 427
FT /evidence="ECO:0000313|EMBL:ACD01600.1"
SQ SEQUENCE 427 AA; 48079 MW; E86B0C7F0B16D597 CRC64;
VPSVKPGYLR PLVPEQAPLQ AEPWTAVMAD IERVVMSGVT HWQSPRFHAY FPTANSYPAI
VADMLSGAIA CIGFTWIASP ACTELEVVML DWLGQMLGLP DQFLARSGGE AGGVIQGTAS
EATLVALLGA KSRMMHRVKE QHPEWSETDI LGKLVGYCNQ QAHSSVERAG LLGGVKLRSL
KPDSKRRLRG DTLREAIDED IRNGLIPFYA VATLGTTSSC AFDALDEIGD VCNASGIWLH
VDAAYAGSAF ICPEYRHLMK GVEKADSFNF NPHKWMLVNF DCSAMWLKQP RWIVDAFNVD
PLYLKHDQQG SAPDYRHWQI PLGRRFRSLK LWFVLRLYGV ENLQNYIRKQ IGFAHLFERL
LTSDERFELF EEVTMGLVCF RLKGSNETNE ELLRRINGRG KIHLVPSKID DVYFLRLAIC
SRFTEES
//
